How, when and why proteins collapse: The relation to folding

Research output: Contribution to journalReview articlepeer-review

Abstract

Unfolded proteins under strongly denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily observed in natively unfolded proteins. Time-resolved studies, using FRET and small-angle scattering, have shown that the collapse transition is a very fast event, probably occurring on the submicrosecond time scale. The forces driving collapse are likely to involve both hydrophobic and backbone interactions. The loss of configurational entropy during collapse makes the unfolded state less stable compared to the folded state, thus facilitating folding.

Original languageEnglish
Pages (from-to)14-20
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume22
Issue number1
DOIs
StatePublished - Feb 2012

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Structural Biology

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